KRBBB_MOUSE
ID KRBBB_MOUSE Reviewed; 223 AA.
AC Q99JB4; Q3TE58; Q497F5; Q7TMP8; Q8BRW0; Q925G5; Q99P32;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Killer cell lectin-like receptor subfamily B member 1B allele B;
DE AltName: Full=CD161 antigen-like family member B;
DE AltName: Full=Inhibitory receptor NKR-P1B;
DE AltName: Full=Lymphocyte antigen 55d;
DE Short=Ly-55d;
DE AltName: Full=NKR-P1D;
DE AltName: Full=Natural killer cell surface protein NKR-P1B allele B6;
DE AltName: CD_antigen=CD161b;
GN Name=Klrb1b; Synonyms=Klrb1d, Ly55d, Nkrp1b, Nkrp1d;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND DOMAIN ITIM MOTIF.
RC STRAIN=C57BL/6J;
RX PubMed=11685472; DOI=10.1007/s002510100367;
RA Plougastel B., Matsumoto K., Dubbelde C., Yokoyama W.M.;
RT "Analysis of a 1-Mb BAC contig overlapping the mouse Nkrp1 cluster of
RT genes: cloning of three new Nkrp1 members, Nkrp1d, Nkrp1e, and Nkrp1f.";
RL Immunogenetics 53:592-598(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6NCr;
RA Carlyle J.R.;
RL Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J;
RA Ryan J.C., Kumar V., Bennett M., Sivakumar P.V., Niemi E.C., Hayashi S.,
RA Nakamura M.C.;
RL Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J;
RA Kung S.K.P., Su R.-C., Shannon J., Miller R.G.;
RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Aorta, Head, and Vein;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6NCr; TISSUE=Hematopoietic stem cell;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=9390275;
RA Appasamy P.M., Kenniston T.W., Brissette-Storkus C.S., Chambers W.H.;
RT "NKR-P1dim/TCR alpha beta + T cells and natural killer cells share
RT expression of NKR-P1A and NKR-P1D.";
RL Nat. Immunol. 15:259-268(1996).
RN [8]
RP FUNCTION, AND SUBUNIT.
RX PubMed=12858173; DOI=10.1038/ni954;
RA Iizuka K., Naidenko O.V., Plougastel B.F.M., Fremont D.H., Yokoyama W.M.;
RT "Genetically linked C-type lectin-related ligands for the NKRP1 family of
RT natural killer cell receptors.";
RL Nat. Immunol. 4:801-807(2003).
RN [9]
RP FUNCTION, AND INTERACTION WITH CLEC2D.
RX PubMed=14990792; DOI=10.1073/pnas.0308304101;
RA Carlyle J.R., Jamieson A.M., Gasser S., Clingan C.S., Arase H.,
RA Raulet D.H.;
RT "Missing self-recognition of Ocil/Clr-b by inhibitory NKR-P1 natural killer
RT cell receptors.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:3527-3532(2004).
RN [10]
RP ANTI-NK1.1 MONOCLONAL ANTIBODY, AND POLYMORPHISM.
RC STRAIN=BALB/cJ; TISSUE=Spleen;
RX PubMed=16751398; DOI=10.4049/jimmunol.176.12.7511;
RA Carlyle J.R., Mesci A., Ljutic B., Belanger S., Tai L.-H., Rousselle E.,
RA Troke A.D., Proteau M.-F., Makrigiannis A.P.;
RT "Molecular and genetic basis for strain-dependent NK1.1 alloreactivity of
RT mouse NK cells.";
RL J. Immunol. 176:7511-7524(2006).
CC -!- FUNCTION: Receptor for CLEC2D/OCIL. Ligand-binding contributes to
CC inhibition of cytotoxic natural killer (NK) cells. May mediate MHC
CC class I-independent 'missing-self' recognition of allografts, tumor
CC cells and virus-infected cells. {ECO:0000269|PubMed:12858173,
CC ECO:0000269|PubMed:14990792}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. Interacts with tyrosine kinase
CC LCK. Binds PTPN6/SHP-1 in a phosphorylation-dependent manner.
CC {ECO:0000269|PubMed:12858173, ECO:0000269|PubMed:14990792}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
CC membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in NK cells and a subset of T-cells.
CC {ECO:0000269|PubMed:9390275}.
CC -!- DOMAIN: Contains 1 copy of a cytoplasmic motif that is referred to as
CC the immunoreceptor tyrosine-based inhibitor motif (ITIM). The
CC phosphorylated ITIM motif can bind the SH2 domain of several SH2-
CC containing phosphatases leading to down-regulation of cell activation.
CC {ECO:0000269|PubMed:11685472}.
CC -!- POLYMORPHISM: Variants Thr-191 and Ala-191 interfere with binding of
CC the anti-NK1.1 monoclonal antibody PK136 which identifies NK cells from
CC C57BL/6 and SJL but not BALB/c mice by binding Klrb1b and Klrb1c in an
CC allele-dependent manner. Mutagenesis of Thr-191 to Ser-191 restores
CC NK1.1 reactivity to Klrb1b from BALB/c mice.
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DR EMBL; AF324825; AAL37353.1; -; Genomic_DNA.
DR EMBL; AF324826; AAL37354.1; -; mRNA.
DR EMBL; AF338321; AAK08512.1; -; mRNA.
DR EMBL; AF338322; AAK08513.1; -; mRNA.
DR EMBL; AF342896; AAK26639.1; -; mRNA.
DR EMBL; AF354260; AAK39100.1; -; mRNA.
DR EMBL; AK030702; BAC27088.1; -; mRNA.
DR EMBL; AK041228; BAC30869.2; -; mRNA.
DR EMBL; AK169820; BAE41390.1; -; mRNA.
DR EMBL; BC055379; AAH55379.1; -; mRNA.
DR EMBL; BC100580; AAI00581.1; -; mRNA.
DR CCDS; CCDS39655.1; -.
DR RefSeq; NP_085102.4; NM_030599.4.
DR PDB; 5TZN; X-ray; 2.60 A; A/W=89-215.
DR PDB; 6E7D; X-ray; 2.90 A; Q/R/S/T/U/V/W/X=89-215.
DR PDBsum; 5TZN; -.
DR PDBsum; 6E7D; -.
DR AlphaFoldDB; Q99JB4; -.
DR SMR; Q99JB4; -.
DR STRING; 10090.ENSMUSP00000032472; -.
DR MEROPS; I63.002; -.
DR MaxQB; Q99JB4; -.
DR PaxDb; Q99JB4; -.
DR PRIDE; Q99JB4; -.
DR ProteomicsDB; 265026; -.
DR DNASU; 80782; -.
DR Ensembl; ENSMUST00000032472; ENSMUSP00000032472; ENSMUSG00000079298.
DR GeneID; 80782; -.
DR KEGG; mmu:80782; -.
DR UCSC; uc009ees.2; mouse.
DR CTD; 80782; -.
DR MGI; MGI:107539; Klrb1b.
DR VEuPathDB; HostDB:ENSMUSG00000079298; -.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00940000154685; -.
DR HOGENOM; CLU_049894_8_2_1; -.
DR OMA; TEIRWIC; -.
DR OrthoDB; 1341815at2759; -.
DR PhylomeDB; Q99JB4; -.
DR TreeFam; TF337735; -.
DR BioGRID-ORCS; 80782; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Klrb1b; mouse.
DR Proteomes; UP000000589; Chromosome 6.
DR Bgee; ENSMUSG00000079298; Expressed in lumbar dorsal root ganglion and 39 other tissues.
DR ExpressionAtlas; Q99JB4; baseline and differential.
DR Genevisible; Q99JB4; MM.
DR GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR GO; GO:0038023; F:signaling receptor activity; IDA:MGI.
DR GO; GO:0045953; P:negative regulation of natural killer cell mediated cytotoxicity; IDA:MGI.
DR GO; GO:0042269; P:regulation of natural killer cell mediated cytotoxicity; IBA:GO_Central.
DR CDD; cd03593; CLECT_NK_receptors_like; 1.
DR Gene3D; 3.10.100.10; -; 1.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR033992; NKR-like_CTLD.
DR Pfam; PF00059; Lectin_C; 1.
DR SMART; SM00034; CLECT; 1.
DR SUPFAM; SSF56436; SSF56436; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Lectin; Membrane; Receptor;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..223
FT /note="Killer cell lectin-like receptor subfamily B member
FT 1B allele B"
FT /id="PRO_0000271479"
FT TOPO_DOM 1..43
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 44..64
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 65..223
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 101..211
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT MOTIF 6..11
FT /note="ITIM motif"
FT MOTIF 32..35
FT /note="LCK-binding motif"
FT DISULFID 122..210
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 189..202
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT CONFLICT 68
FT /note="K -> E (in Ref. 6; AAH55379)"
FT /evidence="ECO:0000305"
FT CONFLICT 78
FT /note="V -> I (in Ref. 6; AAH55379/AAI00581)"
FT /evidence="ECO:0000305"
FT CONFLICT 131
FT /note="L -> P (in Ref. 2; AAK08513)"
FT /evidence="ECO:0000305"
FT CONFLICT 139
FT /note="R -> G (in Ref. 6; AAI00581)"
FT /evidence="ECO:0000305"
FT CONFLICT 146
FT /note="K -> R (in Ref. 2; AAK08513)"
FT /evidence="ECO:0000305"
FT CONFLICT 183
FT /note="V -> D (in Ref. 4; AAK39100)"
FT /evidence="ECO:0000305"
FT CONFLICT 191
FT /note="A -> S (in Ref. 4; AAK39100)"
FT /evidence="ECO:0000305"
FT CONFLICT 191
FT /note="A -> T (in Ref. 5; BAE41390)"
FT /evidence="ECO:0000305"
FT CONFLICT 195
FT /note="E -> D (in Ref. 4; AAK39100 and 5; BAE41390)"
FT /evidence="ECO:0000305"
FT CONFLICT 201
FT /note="G -> S (in Ref. 4; AAK39100 and 5; BAE41390)"
FT /evidence="ECO:0000305"
FT CONFLICT 204
FT /note="S -> T (in Ref. 4; AAK39100 and 5; BAE41390)"
FT /evidence="ECO:0000305"
FT CONFLICT 217
FT /note="E -> K (in Ref. 5; BAE41390)"
FT /evidence="ECO:0000305"
FT CONFLICT 220
FT /note="C -> S (in Ref. 4; AAK39100 and 5; BAE41390)"
FT /evidence="ECO:0000305"
FT CONFLICT 223
FT /note="S -> P (in Ref. 6; AAI00581)"
FT /evidence="ECO:0000305"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:5TZN"
FT STRAND 104..108
FT /evidence="ECO:0007829|PDB:5TZN"
FT HELIX 115..124
FT /evidence="ECO:0007829|PDB:5TZN"
FT HELIX 135..143
FT /evidence="ECO:0007829|PDB:5TZN"
FT STRAND 150..159
FT /evidence="ECO:0007829|PDB:5TZN"
FT TURN 160..163
FT /evidence="ECO:0007829|PDB:5TZN"
FT STRAND 164..167
FT /evidence="ECO:0007829|PDB:5TZN"
FT STRAND 188..193
FT /evidence="ECO:0007829|PDB:5TZN"
FT STRAND 196..200
FT /evidence="ECO:0007829|PDB:5TZN"
FT STRAND 206..213
FT /evidence="ECO:0007829|PDB:5TZN"
SQ SEQUENCE 223 AA; 25027 MW; 369302CAD529CEC3 CRC64;
MDSTTLVYAD LNLARIQEPK HDSPPSLSPD TCRCPRWHRL ALKFGCAGLI LLVLVVIGLC
VLVLSVQKSS VQKICADVQE NRTHTTGCSA KLECPQDWLS HRDKCFHVSQ VSNTWKECRI
DCDKKGATLL LIQDQEELRF LLDSIKEKYN SFWIGLSYTL TDMNWKWING TAFNSDVLKI
TGVTENGSCA AISGEKVTSE GCSSDNRWIC QKELNHETPC NDS
